Proteasome as a Molecular Target of Microcystin-LR
AbstractProteasome degrades proteins in eukaryotic cells. As such, the proteasome is crucial in cell cycle and function. This study proved that microcystin-LR (MC-LR), which is a toxic by-product of algal bloom, can target cellular proteasome and selectively inhibit proteasome trypsin-like (TL) activity. MC-LR at 1 nM can inhibit up to 54% of the purified 20S proteasome TL activity and 43% of the proteasome TL activity in the liver of the cyprinid rare minnow (Gobiocypris rarus). Protein degradation was retarded in GFP-CL1-transfected PC-3 cells because MC-LR inhibited the proteasome TL activity. Docking studies indicated that MC-LR blocked the active site of the proteasome β2 subunit; thus, the proteasome TL activity was inhibited. In conclusion, MC-LR can target proteasome, selectively inhibit proteasome TL activity, and retard protein degradation. This study may be used as a reference of future research on the toxic mechanism of MC-LR. View Full-Text
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Zhu, Z.; Zhang, L.; Shi, G. Proteasome as a Molecular Target of Microcystin-LR. Toxins 2015, 7, 2221-2231.
Zhu Z, Zhang L, Shi G. Proteasome as a Molecular Target of Microcystin-LR. Toxins. 2015; 7(6):2221-2231.Chicago/Turabian Style
Zhu, Zhu; Zhang, Li; Shi, Guoqing. 2015. "Proteasome as a Molecular Target of Microcystin-LR." Toxins 7, no. 6: 2221-2231.